PUR4_VIBPA
ID PUR4_VIBPA Reviewed; 1302 AA.
AC Q87RW0;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000255|HAMAP-Rule:MF_00419};
DE Short=FGAM synthase {ECO:0000255|HAMAP-Rule:MF_00419};
DE Short=FGAMS {ECO:0000255|HAMAP-Rule:MF_00419};
DE EC=6.3.5.3 {ECO:0000255|HAMAP-Rule:MF_00419};
DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase {ECO:0000255|HAMAP-Rule:MF_00419};
DE Short=FGAR amidotransferase {ECO:0000255|HAMAP-Rule:MF_00419};
DE Short=FGAR-AT {ECO:0000255|HAMAP-Rule:MF_00419};
GN Name=purL {ECO:0000255|HAMAP-Rule:MF_00419}; OrderedLocusNames=VP0666;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
CC -!- FUNCTION: Phosphoribosylformylglycinamidine synthase involved in the
CC purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of
CC formylglycinamide ribonucleotide (FGAR) and glutamine to yield
CC formylglycinamidine ribonucleotide (FGAM) and glutamate.
CC {ECO:0000255|HAMAP-Rule:MF_00419}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-
CC ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-
CC ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate;
CC Xref=Rhea:RHEA:17129, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:147286, ChEBI:CHEBI:147287,
CC ChEBI:CHEBI:456216; EC=6.3.5.3; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00419};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-
CC phospho-D-ribosyl)glycinamide: step 1/2. {ECO:0000255|HAMAP-
CC Rule:MF_00419}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00419}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00419}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the FGAMS family.
CC {ECO:0000255|HAMAP-Rule:MF_00419}.
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DR EMBL; BA000031; BAC58929.1; -; Genomic_DNA.
DR RefSeq; NP_797045.1; NC_004603.1.
DR RefSeq; WP_005455948.1; NC_004603.1.
DR AlphaFoldDB; Q87RW0; -.
DR SMR; Q87RW0; -.
DR STRING; 223926.28805652; -.
DR EnsemblBacteria; BAC58929; BAC58929; BAC58929.
DR GeneID; 1188141; -.
DR KEGG; vpa:VP0666; -.
DR PATRIC; fig|223926.6.peg.634; -.
DR eggNOG; COG0046; Bacteria.
DR eggNOG; COG0047; Bacteria.
DR HOGENOM; CLU_001031_0_2_6; -.
DR OMA; LSANWMW; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000002493; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1330.10; -; 2.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.90.650.10; -; 2.
DR HAMAP; MF_00419; PurL_1; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR040707; FGAR-AT_N.
DR InterPro; IPR010073; PurL_large.
DR InterPro; IPR041609; PurL_linker.
DR InterPro; IPR010918; PurM-like_C_dom.
DR InterPro; IPR036676; PurM-like_C_sf.
DR InterPro; IPR036921; PurM-like_N_sf.
DR InterPro; IPR036604; PurS-like_sf.
DR Pfam; PF02769; AIRS_C; 2.
DR Pfam; PF18072; FGAR-AT_linker; 1.
DR Pfam; PF18076; FGAR-AT_N; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF55326; SSF55326; 2.
DR SUPFAM; SSF56042; SSF56042; 2.
DR SUPFAM; SSF82697; SSF82697; 1.
DR TIGRFAMs; TIGR01735; FGAM_synt; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Glutamine amidotransferase; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT CHAIN 1..1302
FT /note="Phosphoribosylformylglycinamidine synthase"
FT /id="PRO_0000100421"
FT DOMAIN 1049..1302
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1142
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1267
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1269
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 307..318
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 678
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 718
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 722
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 891
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
SQ SEQUENCE 1302 AA; 141687 MW; 00C5C7FD41595FB1 CRC64;
MRILRGSPAL SEFRVNKLLE LCREQDLPVT GIYAEFMHFA DLKSDLDDQE LEKLEKLLTY
GPTIEEHEPE GLLLLVTPRP GTISPWSSKS TDIAINCGLD TVKRLERGTA YYVESSVVLS
EAQVDAVKAL IHDRMMETVF TELEAASALF TVAEPKPVAH VDILAGGRLA LEEANVSLGL
ALAEDEIDYL VENFTKLGRN PNDIELMMFA QANSEHCRHK IFNADWTIDG VDQEKSLFKM
IKNTFETTPD HVLSAYKDNA AVMTGSKVGR FFPDPKSRQY TYHHEDAHIL MKVETHNHPT
AISPWPGAST GSGGEIRDEG ATGIGGKPKA GLVGFTTSNL RIPGFEQPWE TDFGKPGRIV
NALDIMLEGP LGGAAFNNEF GRPNLLGYFR TYEEKVTSHA GEEVRGYHKP IMIAGGMGNI
RDEHVQKKEI PVGASLIVLG GPAMNIGLGG GAASSMASGQ SAEDLDFASV QRENPEMERR
CQEVIDRCWQ LGEENPIAFI HDVGAGGISN ALPELCDDGE RGGKFQLRDV PNDELSMSPL
EIWCNESQER YVLAVAPENM EAFDAICKRE RAPYAVVGVA TEERHLTLED SHFDNTPIDM
PMDILLGKTP KMHREATTLK VDSPAIARDG IEIDEAADRV LRLPTVAEKT FLITIGDRSV
TGLVARDQMV GPWQVPVANC AVTAASYDTY HGEAMSMGER TPVALLDFGA SARLAVGESL
TNIAATDIGD IKRIKLSANW MSPAGHPGED AGLYEAVKAV GEELCPALGL TIPVGKDSMS
MKTKWEENGE SKEVTSPLSL VITAFGRVED VRKTVTPQLR TSDTLEGLGD TSLVLVDLGN
GKNRLGATAL AQVYKQLGDK PADVDNAEQL KGFFDAMQNL VRNDKLLAYH DKGDGGLFVT
LAEMAFAGHC GVKADIAELG EDALAVLFNE ELGAVVQVKN DDLDSVLSTL AANGLEACSH
VIGSVEASDD FVFTSGDDVV LKRSRTELRV IWAETTHKMQ ALRDNPACAD QEFEAKKDNT
DPGLNVSLSF DVNEDIAAPY IAKGAKPKMA ILREQGVNSH VEMAAAFDRA GFEATDIHMS
DILTGQAVLD EYQGLVACGG FSYGDVLGAG EGWAKSILFN AQAREQFQAF FNREETFSLG
VCNGCQMLSN LKELIPGADL WPRFVRNESE RFEARFSLVE VQKSDSVFFD GMAGSRMPIA
VSHGEGRVEV RDGEHLNAIE ASGTVALRYV DNNGNPTQQY PNNPNGSPNA ITGLTTADGR
VTIMMPHPER VFRTVANSWA PEGWGENGAW MRMFQNARKN IG
